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http://hdl.handle.net/10553/76675
Title: | Superóxido dismutasa y catalasa en batterias bioluminiscentes marinas | Other Titles: | Superoxide dismutase and catalase in marine bioluminescent bacteria | Authors: | González-Lama, Zoilo Díez del Pino, A. |
UNESCO Clasification: | 2414 Microbiología | Keywords: | Bioluminescent Bacteria Catalase Photobacterium Superoxide Dismutase Vibrio |
Issue Date: | 1996 | Journal: | Boletín - Instituto Español de Oceanografía | Abstract: | Catalase and superoxide dismutase (SOD) were studied in strains of marine bioluminescent bacteria. We found several isozymes of catalase in these strains and only one isozyme of superoxide dismutase. We observed that catalase levels rose as bioluminiscence emission fell. A dark strain ofPhotobacterium phosphoreum var. K showed the maximun levels of catalase. There are two types of catalases in this strain: an isozyme of pI 7.2 inhibited by 3-amino, 1, 2, 4-triazole and others isozymes resistent to this inhibitor. All isozymes of catalase from these bioluminescent marine bacteria are hemo-proteins, since they were inhibited by cianyde and azide. The single isozyme of SOD is a Fe-SOD. Han sido estudiadas la catalasa y la superóxido dismutasa (SOD) de bacterias bioluminiscentes marinas. Hemos encontrado varios isoenzimas de catalasa y un isoenzima de superóxido dismutasa y se ha observado que a menor luminiscencia los niveles de catalasa son mayores. Una variante de Photobacterium phosphoreum var K (cepa mutante que carece de bioluminiscencia) mostró los múximos niveles de catalasa. Hay dos tipos de catalasas en esta estirpe, una de pI 7, 2 que es inhibida por el 3-amino, 1, 2, 4-triazol y otros isoenzimas que son resistentes a la acción de este inhibidor. Todas las cata1asa de estas bacterias bioluminiscentes marinas son hemoproteínas, ya que son inhibidas por la azida y el cianuro. El isoenzima de SOD es una Fe-SOD. |
URI: | http://hdl.handle.net/10553/76675 | ISSN: | 0074-0195 | Source: | Boletin - Instituto Español de Oceanografía [ISSN 0074-0195], v. 12 (2), p. 131-137, (Diciembre 1996) |
Appears in Collections: | Artículos |
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